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Two sets of pyridine derivatives that were isosteric substrates for the two activities were differentially affected. Acetazolamide and salamide are reversible inhibitors of the enzyme; only salamide affords protection of the hydrolase activity against the action of C<jats:sub>2<\/jats:sub>N<jats:sub>2<\/jats:sub>. Since each is known to bind in different positions within the active site, the selective effect of salamide may arise from its position covering one CO<jats:sub>2<\/jats:sub> site as well as a site important for hydrolase activity. The C<jats:sub>2<\/jats:sub>N<jats:sub>2<\/jats:sub> concentration dependence of the time course of hydrolase inhibition is consistent with the existence of a high C<jats:sub>2<\/jats:sub>N<jats:sub>2<\/jats:sub> affinity site with slow covalent change and a second site with lower C<jats:sub>2<\/jats:sub>N<jats:sub>2<\/jats:sub> affinity, but higher rate of covalent modification of the enzyme. \u00a9 1993 John Wiley &amp; Sons, Inc.<\/jats:p>","DOI":"10.1002\/bip.360330417","type":"journal-article","created":{"date-parts":[[2004,12,30]],"date-time":"2004-12-30T03:05:43Z","timestamp":1104375943000},"page":"687-692","source":"Crossref","is-referenced-by-count":4,"title":["Cyanogen as a selective probe for carbonic anhydrase hydrolase activity"],"prefix":"10.1002","volume":"33","author":[{"given":"A. 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